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10 p, 1.6 MB |
Cells alter their tRNA abundance to selectively regulate protein synthesis during stress conditions
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Torrent Burgas, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Chalancon, Guilhem (Medical Research Council. Laboratory of Molecular Biology) ;
Sánchez de Groot, Natalia (Medical Research Council. Laboratory of Molecular Biology) ;
Wuster, Arthur (Medical Research Council. Laboratory of Molecular Biology) ;
Babu, Madam M. (Medical Research Council. Laboratory of Molecular Biology)
Decoding the information in mRNA during protein synthesis relies on tRNA adaptors, the abundance of which can affect the decoding rate and translation efficiency. To determine whether cells alter tRNA abundance to selectively regulate protein expression, we quantified changes in the abundance of individual tRNAs at different time points in response to diverse stress conditions in Saccharomyces cerevisiae. [...]
2018 -  10.1126/scisignal.aat6409
Science Signaling, Vol. 11, Issue 546 (September 2018) , art. eaat6409
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14 p, 3.1 MB |
RNA-binding and prion domains : the Yin and Yang of phase separation
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Gotor, Nieves Lorenzo (Centre de Regulació Genòmica) ;
Armaos, Alexandros (Centre de Regulació Genòmica) ;
Calloni, Giulia (Goethe University Frankfurt) ;
Torrent Burgas, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Vabulas, R. Martin (Goethe University Frankfurt) ;
Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ;
Tartaglia, Gian Gaetano (Centre de Regulació Genòmica)
Proteins and RNAs assemble in membrane-less organelles that organize intracellular spaces and regulate biochemical reactions. The ability of proteins and RNAs to form condensates is encoded in their sequences, yet it is unknown which domains drive the phase separation (PS) process and what are their specific roles. [...]
2020 - 10.1093/nar/gkaa681
Nucleic acids research, Vol. 48, Issue 17 (September 2020) , p. 9491-9504
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13 p, 5.2 MB |
Discovering putative prion-like proteins in Plasmodium falciparum : a computational and experimental analysis
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Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ;
Iglesias, Valentin (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Biosca, Arnau (Institut de Bioenginyeria de Catalunya) ;
Fernàndez-Busquets, Xavier (Institut de Bioenginyeria de Catalunya) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prions are a singular subset of proteins able to switch between a soluble conformation and a self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases, increasing evidence indicates that organisms exploit prion-like mechanisms for beneficial purposes. [...]
2018 - 10.3389/fmicb.2018.01737
Frontiers in microbiology, Vol. 9 (Aug. 2018) , art. 1737
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20 p, 3.5 MB |
The fitness cost and benefit of phase-separated protein deposits
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Sánchez de Groot, Natalia (Centre de Regulació Genòmica) ;
Torrent Burgas, Marc (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Ravarani, Charles N. J. (Medical Research Council Laboratory of Molecular Biology) ;
Trusina, Ala (Niels Bohr Institute) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Babu, Madam M (Medical Research Council Laboratory of Molecular Biology)
Phase separation of soluble proteins into insoluble deposits is associated with numerous diseases. However, protein deposits can also function as membrane-less compartments for many cellular processes. [...]
2019 - 10.15252/msb.20178075
Molecular systems biology, Vol. 15, issue 4 (April 2019) , art. e8075
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10 p, 1.3 MB |
Characterization of Amyloid Cores in Prion Domains
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Sant'Anna, Ricardo (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Fernández Gallegos, María Rosario (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Navarro, Susanna (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ;
Serpell, Louise (University of Sussex. School of Life Sciences) ;
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloids consist of repetitions of a specific polypeptide chain in a regular cross-β-sheet conformation. Amyloid propensity is largely determined by the protein sequence, the aggregation process being nucleated by specific and short segments. [...]
2016 - 10.1038/srep34274
Scientific reports, Vol. 6 (2016) , art. 34274
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